ID   A0A076MLG9_AMYME        Unreviewed;       212 AA.
AC   A0A076MLG9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Phosphoenolpyruvate guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_02114};
DE            Short=PEP guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_02114};
DE            EC=2.7.7.105 {ECO:0000256|HAMAP-Rule:MF_02114};
GN   Name=fbiD {ECO:0000256|HAMAP-Rule:MF_02114};
GN   ORFNames=AMETH_1531 {ECO:0000313|EMBL:AIJ21623.1};
OS   Amycolatopsis methanolica 239.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis; Amycolatopsis methanolica group.
OX   NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ21623.1, ECO:0000313|Proteomes:UP000062973};
RN   [1] {ECO:0000313|EMBL:AIJ21623.1, ECO:0000313|Proteomes:UP000062973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=239 {ECO:0000313|EMBL:AIJ21623.1,
RC   ECO:0000313|Proteomes:UP000062973};
RA   Tang B.;
RT   "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Guanylyltransferase that catalyzes the activation of
CC       phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via
CC       the condensation of PEP with GTP. It is involved in the biosynthesis of
CC       coenzyme F420, a hydride carrier cofactor. {ECO:0000256|HAMAP-
CC       Rule:MF_02114}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H(+) + phosphoenolpyruvate = diphosphate + enolpyruvoyl-
CC         2-diphospho-5'-guanosine; Xref=Rhea:RHEA:30519, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58702,
CC         ChEBI:CHEBI:143701; EC=2.7.7.105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02114};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02114}.
CC   -!- SIMILARITY: Belongs to the CofC family. {ECO:0000256|HAMAP-
CC       Rule:MF_02114}.
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DR   EMBL; CP009110; AIJ21623.1; -; Genomic_DNA.
DR   RefSeq; WP_017987483.1; NZ_CP009110.1.
DR   AlphaFoldDB; A0A076MLG9; -.
DR   STRING; 1068978.AMETH_1531; -.
DR   KEGG; amq:AMETH_1531; -.
DR   PATRIC; fig|1068978.7.peg.1613; -.
DR   eggNOG; COG1920; Bacteria.
DR   HOGENOM; CLU_076569_0_0_11; -.
DR   OrthoDB; 9151145at2; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000062973; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043814; F:phospholactate guanylyltransferase activity; IEA:InterPro.
DR   GO; GO:0052645; P:F420-0 metabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02114; CofC; 1.
DR   InterPro; IPR002835; CofC.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   NCBIfam; TIGR03552; F420_cofC; 1.
DR   PANTHER; PTHR40392; 2-PHOSPHO-L-LACTATE GUANYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR40392:SF1; 2-PHOSPHO-L-LACTATE GUANYLYLTRANSFERASE; 1.
DR   Pfam; PF01983; CofC; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_02114};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02114};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_02114,
KW   ECO:0000313|EMBL:AIJ21623.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062973};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02114, ECO:0000313|EMBL:AIJ21623.1}.
FT   BINDING         142
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
FT   BINDING         158
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
FT   BINDING         161
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
SQ   SEQUENCE   212 AA;  21635 MW;  C519EBA094888349 CRC64;
     MPVPVEISGL IVPLKPPRAG KSRLRGAVDE HDHAALVLAL AWDTLAAATD AGVRRVLVVA
     ADPAAVSGLR RPGVEVVGER GDGDLNSALR QGEALLRQRE PDAVVGAIQA DLPALRPAEL
     AAALAAAEGR RVFVADADGT GTTLLLSEPG GPLDPRFGAG SAAAHAGSGA VPLELDLPTL
     RRDVDTPADL AEACRLGVGD RTRAVLCSRE VA
//